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• W133056582 abstract "Research Article1 September 1994free access The catalytic activity of the CD45 membrane-proximal phosphatase domain is required for TCR signaling and regulation. D.M. Desai D.M. Desai Howard Hughes Medical Institute, Department of Medicine, University of California at San Francisco 94143-0724. Search for more papers by this author J. Sap J. Sap Howard Hughes Medical Institute, Department of Medicine, University of California at San Francisco 94143-0724. Search for more papers by this author O. Silvennoinen O. Silvennoinen Howard Hughes Medical Institute, Department of Medicine, University of California at San Francisco 94143-0724. Search for more papers by this author J. Schlessinger J. Schlessinger Howard Hughes Medical Institute, Department of Medicine, University of California at San Francisco 94143-0724. Search for more papers by this author A. Weiss A. Weiss Howard Hughes Medical Institute, Department of Medicine, University of California at San Francisco 94143-0724. Search for more papers by this author D.M. Desai D.M. Desai Howard Hughes Medical Institute, Department of Medicine, University of California at San Francisco 94143-0724. Search for more papers by this author J. Sap J. Sap Howard Hughes Medical Institute, Department of Medicine, University of California at San Francisco 94143-0724. Search for more papers by this author O. Silvennoinen O. Silvennoinen Howard Hughes Medical Institute, Department of Medicine, University of California at San Francisco 94143-0724. Search for more papers by this author J. Schlessinger J. Schlessinger Howard Hughes Medical Institute, Department of Medicine, University of California at San Francisco 94143-0724. Search for more papers by this author A. Weiss A. Weiss Howard Hughes Medical Institute, Department of Medicine, University of California at San Francisco 94143-0724. Search for more papers by this author Author Information D.M. Desai1, J. Sap1, O. Silvennoinen1, J. Schlessinger1 and A. Weiss1 1Howard Hughes Medical Institute, Department of Medicine, University of California at San Francisco 94143-0724. The EMBO Journal (1994)13:4002-4010https://doi.org/10.1002/j.1460-2075.1994.tb06716.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Cell surface expression of CD45, a receptor-like protein tyrosine phosphatase (PTPase), is required for T cell antigen receptor (TCR)-mediated signal transduction. Like the majority of transmembrane PTPases, CD45 contains two cytoplasmic phosphatase domains, whose relative in vivo function is not known. Site-directed mutagenesis of the individual catalytic residues of the two CD45 phosphatase domains indicates that the catalytic activity of the membrane-proximal domain is both necessary and sufficient for restoration of TCR signal transduction in a CD45-deficient cell. The putative catalytic activity of the distal phosphatase domain is not required for proximal TCR-mediated signaling events. Moreover, in the context of a chimeric PTPase receptor, the putative catalytic activity of the distal phosphatase domain is not required for ligand-induced negative regulation of PTPase function. We also demonstrate that the phosphorylation of the C-terminal tyrosine of Lck, a site of negative regulation, is reduced only when CD45 mutants with demonstrable in vitro phosphatase activity are introduced into the CD45-deficient cells. These results demonstrate that the phosphatase activity of CD45 is critical for TCR signaling, and for regulating the levels of C-terminal phosphorylated Lck molecules. Previous ArticleNext Article Volume 13Issue 171 September 1994In this issue RelatedDetailsLoading ..." @default.
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• W133056582 title "The catalytic activity of the CD45 membrane-proximal phosphatase domain is required for TCR signaling and regulation." @default.
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• W133056582 doi "https://doi.org/10.1002/j.1460-2075.1994.tb06716.x" @default.
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